Decreasing the Basicity of the Active Site Base, Lys-258, of Escherichia coli Aspartate Aminotransferase by Replacement with .gamma.-thialysine

Biochemistry ◽  
1995 ◽  
Vol 34 (12) ◽  
pp. 3990-3998 ◽  
Author(s):  
Lisa M. Gloss ◽  
Jack F. Kirsch
Keyword(s):  
Escherichia Coli ◽  
Active Site ◽  
Aspartate Aminotransferase

2.8-.ANG.-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli

Biochemistry ◽  
1989 ◽  
Vol 28 (20) ◽  
pp. 8161-8167 ◽  
Author(s):  
Douglas L. Smith ◽  
Steven C. Almo ◽  
Michael D. Toney ◽  
Dagmar Ringe
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Active Site ◽  
Aspartate Aminotransferase

Activity and structure of the active-site mutants R386Y and R386F of Escherichia coli aspartate aminotransferase

Biochemistry ◽  
1991 ◽  
Vol 30 (7) ◽  
pp. 1980-1985 ◽  
Author(s):  
Avis T. Danishefsky ◽  
James J. Onnufer ◽  
Gregory A. Petsko ◽  
Dagmar Ringe
Keyword(s):  
Escherichia Coli ◽  
Active Site ◽  
Aspartate Aminotransferase ◽  
Active Site Mutants

scholarly journals Formate-induced Labeling of the Active Site of Aspartate Aminotransferase by β-Chloro-l-alanine

1974 ◽  
Vol 249 (20) ◽  
pp. 6684-6692
Author(s):  
Yoshimasa Morino ◽  
Abdalla Mohamed Osman ◽  
Mitsuhiro Okamoto
Keyword(s):  
Active Site ◽  
Aspartate Aminotransferase
Sign in / Sign up

Export Citation Format

Share Document